Non-allosteric enzyme switches possess larger effector-induced changes in thermodynamic stability than their non-switch analogs

Protein Science

Volumn 22, Issue 4, 2013, Pages 475-485

  Choi, Jay H ^a   San, Angela ^a   Ostermeier, Marc ^a  

^a Johns Hopkins University   (United States)

Author keywords

lactamase; Allostery; Domain fusion; Maltose binding protein; Phenotypic switch; Protein switch

Indexed keywords

BETA LACTAMASE; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; PROTEIN TEM1 BETA LACTAMASE; UNCLASSIFIED DRUG;

ARTICLE; BIOTECHNOLOGY; CELL INTERACTION; IN VIVO STUDY; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN UNFOLDING;

ALLOSTERIC REGULATION; BETA-LACTAMASES; MALTOSE-BINDING PROTEINS; PHENOTYPE; PROTEIN ENGINEERING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; PROTEOLYSIS; RECOMBINANT FUSION PROTEINS; THERMODYNAMICS;

EID: 84878323463     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2234     Document Type: Article

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